ID E1WL07_BACF6 Unreviewed; 479 AA.
AC E1WL07;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=frrD {ECO:0000313|EMBL:CBW21170.1};
GN OrderedLocusNames=BF638R_0581 {ECO:0000313|EMBL:CBW21170.1};
OS Bacteroides fragilis (strain 638R).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=862962 {ECO:0000313|EMBL:CBW21170.1, ECO:0000313|Proteomes:UP000008560};
RN [1] {ECO:0000313|EMBL:CBW21170.1, ECO:0000313|Proteomes:UP000008560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=638R {ECO:0000313|EMBL:CBW21170.1,
RC ECO:0000313|Proteomes:UP000008560};
RX PubMed=20829291; DOI=10.1099/mic.0.042978-0;
RA Patrick S., Blakely G.W., Houston S., Moore J., Abratt V.R., Bertalan M.,
RA Cerdeno-Tarraga A.M., Quail M.A., Corton N., Corton C., Bignell A.,
RA Barron A., Clark L., Bentley S.D., Parkhill J.;
RT "Twenty-eight divergent polysaccharide loci specifying within- and amongst-
RT strain capsule diversity in three strains of Bacteroides fragilis.";
RL Microbiology 156:3255-3269(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
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DR EMBL; FQ312004; CBW21170.1; -; Genomic_DNA.
DR RefSeq; WP_008658371.1; NC_016776.1.
DR AlphaFoldDB; E1WL07; -.
DR KEGG; bfg:BF638R_0581; -.
DR PATRIC; fig|862962.3.peg.596; -.
DR HOGENOM; CLU_000445_89_2_10; -.
DR Proteomes; UP000008560; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CBW21170.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 49..71
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 73..125
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 134..201
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 264..479
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 479 AA; 54017 MW; 0B5BDDF41BAE95EA CRC64;
MNIKTKLLFG IGILAGMIIL LVTLSVVNLQ ILTATEPDSP VAMPALERAL LWISVTGGIC
ILTGLVLLIW LPRSINRPVK ELTCGILEIA NHNYEKRLDM RGYEEFREVS DSFNRMAEKL
TEYRDSTLAD ILSAKKFLEA VVNSIHEPII GLNTEREILF VNNEALNVLN MKRENVIRKS
AEELSLKNDL LRRLIRELVT PGEKNEPLKI YADNKESYFQ ASYIPIENAA AEEGEARNLG
DVILLKNITE FKELDSAKTT FISTISHELK TPISAIMMSL QLLEDKRVGS LNGEQEQLSK
NIRDNSQRLL DITGELLNMT QVEAGKLQMM PKITKPIELI EYAIKANQVQ ADKFNIQIEV
DYPQEKIPKL FVDSEKIAWV LTNLLSNAIR YSKENGRVVI GVRHKKEYIE LYVQDFGKGI
DPRYHQSIFD RYFRVPGTKV QGSGLGLSIS KDFVEAHGGT LTVQSEPGKG SCFVIRLKA
//
